Академический Документы
Профессиональный Документы
Культура Документы
CHAPTER 4
DO YOU KNOW THAT ALL LIVING AND NON-LIVING THINGS ARE MADE SUBSTANCES CALLED ELEMENTS ?
4% of body mass
Trace element Trace element are elements required in very small amounts (0.01 % of body mass), such as zinc, manganese, cobalt, copper, iodine, boron, chromium, molybdenum, selenium and fluorine.
Compounds in The Cell 1. Compounds in living things can be divided int two types: 2. Organic compounds which contain carbon; they are carbohydrate, protein, lipids and nucleic acids. 3. Inorganic compounds such as water.
1. i. ii.
Two types of nucleic acids; DNA (deoxyribonucleic acids) RNA (ribonucleic acids)
Transport medium Medium for biochemical reactions Helps in lubrication Very high *cohesion
*Cohesion The force of attraction between like molecules. Provides the force that holds up a column of water in the xylem tissue of plant without breaking.
4.2 Carbohydrates
1.
2.
a) b) c)
Carbohydrates contain carbon, hydrogen and oxygen. The ratio of hydrogen atom to oxygen atom is 2:1 Three types of carbohydrates: Monosaccharide Disaccharide polysaccharide
a) i. ii. iii. 1.
Monosaccharides They are *monomers of carbohydrate. They are simple sugars. Examples are Glucose found in plants and animals. It is the energy source for cellular respiration. Fructose found in fruits and honey. Galactose present in milk
2.
3.
iv.
v.
They are *reducing sugars. Their presences can be detected using Benedicts test.
Disaccharides They are formed when two monosaccharide combine by condensation (removal of water). For example; Maltose formed from condensation of two glucose molecules.
Glucose + Glucose condensation Maltose + water
Sucrose
hydrolysis
Maltose
non-reducing sugar
*Monomer A molecule that consist of a single unit and can join with others in forming a dimer, trimer or polymer.
*Reducing Sugar A monosaccharide or disaccharide sugar that can donate electrons to other molecules and can therefore act as a reducing agent. *Non-Reducing Sugar A sugar that cannot donate electrons to other molecules and therefore cannot act as a reducing agent.
Polysaccharides
1.
2. 3. i. ii. iii.
They are formed when more than two (up to hundred) of monosaccharides combine through condensation. They are polymers formed by the condensation of glucose molecules. Characteristic of polysacharides: Insoluble in water Do not taste sweet Do not crystsllise
hydrolysis Polysaccharides + Water Monosaccharides
Example i. Starch Storage carbohydrate in plants ii. Glycogen Storage carbohydrate in animal and yeast iii. Cellulose Structural polysaccharides in plant cell Make up the cell wall of plant cells.
4.
5.
They can be broken down into smaller molecules through hydrolysis using dilute acid or enzymes.
4.3 Proteins
1. 2. 3. 4.
5.
They are made up of carbon, hydrogen, oxygen and nitrogen. Some proteins contains sulphur and phosphorus. Proteins are made up of monomers called amino acids. Two molecules of amino acids are joined by a peptide bond to form a dipeptide through *condensation. A dipeptide can be broken down into amino acids by hydrolysis.
*condensation = a chemical reaction in which two molecules combine to form a larger molecule with the elimination of a small molecule.
Amino acid + Amino acid
6. 7.
condensation
hydrolysis
dipeptide + water
8.
9.
Polypeptides are formed when many amino acids are joined together by condensation. Proteins or polypeptides can be broken down through hydrolysis into amino acids. There are 20 types of amino acids in cells. Proteins can be grouped into four levels of organisation according to their structures:
a) b) c) d)
a)
Primary structure This is a linear sequence of amino acids in a polypeptide. Secondary structure The polypeptide is coiled to form an alpha helix or folded into beta-pleated sheets.
c)
c)
Tertiary structure The helix or beta-pleated sheets are folded in many ways into a three dimensional shape of a polypeptide. Examples are hormones, enzymes, antibodies and plasma proteins.
Quarternary structure Two or more tertiary structure polypeptide chains combine to form a large and complex protein molecule. Examples is haemoglobin
d)
Amino acid can be divide into essential amino acid and non essential amino acid. Essential amino acids are amino acids that cannot be synthesised by the body They can only be obtained from diet. Example is leucine. Non-essential amino acid are amino acid that can be synthesised by the body. They are derived from other amino acid. There are 11 non-essential amino acid.
Essential Isoleucine
Nonessential Alanine
Leucine
Lysine Methionine Phenylalanine Threonine Tryptophan
Arginine
Aspartate Cysteine Glutamate Glutamine Glycine
Valine
Histidine Tyrosine Selenocysteine
Proline
Serine Asparagine Pyrrolysine
4.4 Lipids
1.
2.
3.
4.
Lipids contain carbon, hydrogen and oxygen The ratio of hydrogen atoms to oxygen atoms in a lipid molecule is higher than the 2:1 ratio in carbohydrates. Lipid are non-polar molecules. They are insoluble in water but dissolve in ethanol and ether. Important of lipids: Store energy act as sources of energy. Reduce the loss of water by evaporation.
5.
a) b)
c)
d) e)
Lipids (C, H, O )
Waxes
Phospholipids
Component of plasma membrane
Steroids
1. Hormones 2. Cholesterol
Waxes 1. Found on the cuticles of the leaf epidermis, fruits and seeds 2. Waterproof the external surface of plant 3. Protective covering on an insect body. Steroids 1. Include cholesterol and hormones such as testosterone, oestrogen and progesterone
3.
Fats and oils are Triglycerides A triglycerides is formed from glycerol and three molecules of fatty acids through condensation. Triglycerides can be broken down into fatty acids and glycerol by hydrolysis.
glycerol condensation + 3 molecules of Fatty acids hydrolysis triglycerides + 3 molecules of water
4.
Each fatty acids consist of a long hydrocarbon chain with a different number of carbon atoms for different fatty acids.
1. a) b)
a.
Fats containing saturated fatty acids Do not have any double bonds between the carbon atoms. Cannot form any chemical bonds with other atoms. Are solids at room temperature Has more cholesterol
vi.
All the bond between the carbon atoms have the maximum number of hydrogen atoms.
b)
Unsaturated fats
i.
ii.
iii.
Fats containing unsaturated fatty acids Contains fatty acids that have at least one double bond between the carbon atoms. Carbon atoms in the hydrocarbon chain are not bonded to the maximum number of hydrogen atoms.
Usually liquid at room temperature Is called oil Has less cholesterol Unsaturated fats with one double bond are called monounsaturated fats. With two or more double bonds are called polyunsaturated fats.
QUIZ
State
two general characteristics of lipids What is a triglyceride? Name the types of lipids? State the function of steroids and phospholipids? What are saturated fats? What would happen to a person whose diet is always rich in saturated fats?
4.5 Enzymes
1.
2.
Enzymes are biological catalysts that increase the rate of a biochemical reactions in the cells. Enzymes are required by every biochemical reaction to enable the reaction to take place rapidly in the cells at body temperature.
enzyme
Substrate
products
Can be reused
ENZYMES
Protein
Reused
Unchanged Speed
up Reversible Small amount Need cofactor to function Sensitive to Temperature and pH Only catalyse one kind of substrate Have active site to specific substrate. Reaction slowed or stopped cause Inhibitor
Naming of Enzymes
1. 2. a) b) c)
Adding the suffix -ase at the end of the of their substrates. Example: Lactose Lactase Sucrose Sucrase Lipid Lipase
The site of enzymes synthesis Enzymes are protein therefore ribosomes are also the sites of enzymes synthesis. Intracellular and extracellular enzymes 1. Enzymes are synthesised by specific cells. a) Intracellular enzymes = enzymes which are synthesised and retained in the cell for the use of the cell itself. b) Extracellular enzymes = are synthesised in the cell but secreted from the cell to work externally. Example : Lipase and Trypsin
1.
DNA transcribed the instruction for making the extracellular enzymes to RNA.
2.
3. 4.
The mRNA leaves the nucleus and at attaches itself to the ribosome on the Endoplasmic Reticulum. Enzymes/protein are synthesized in Ribosomes.
When the enzymes synthesis has complete, transport through Rough Endoplasmic Reticulum. The enzymes is encapsulated in a Transport Vesicle and fuse with the membrane of the Golgi Apparatus.
5.
6.
In the Golgi Apparatus the enzymes/protein is modified before being sent to the Plasma membrane. The enzymes is packed in a Secretory Vesicle. The Secretory Vesicle membrane fuses with the Plasma Membrane. The enzymes is released outside the cell.
7.
8. 9.
Describe
how the different cellular component are involve in the secretion of this enzymes. ( 10 marks)
building up reaction (synthesis) Two substrate molecules (A and B) which can fit into active site. The shape of the substrate must fit the enzymes precisely if a reaction is to be catalysed.
Lock
and key hypothesis The substrate fits into enzyme is like the key that fits into the locks. The substrate molecule binds to the active site to form an enzymessubstrate complex. The enzymes catalyses the substrate to from product, which then leaves the active site. The enzyme molecule is now free to bind to more substrate molecules.
Quiz
1.
i. ii.
iii.
Identify W, X, Y and Z. State two characteristic of X which are illustrated in figure 1. Name the mechanism of enzymes action illustrated in figure 1.
Briefly explain the mechanism that you have mentioned in (iii). State one use of lipase in a food industry. Explain how enzymes are used. explain what would happen if the temperature of an enzymes-catalysed reaction is increased to more than 60C.
STEP
Temperature
Low temperature 1. At low temperature, enzymes catalysed reaction is slow. 2. The movement of substrate molecules is inactive.
High temperature 1. Enzymes-catalysed reaction will stop. 2. This is because the chemical bonds that hold molecules will break at high temperature 3. Three dimensional shape of enzymes will alter and no longer fit the substrate molecule.
Optimum temperature Is the temperature where an enzymes catalyses a maximum reaction. The temperature causes rapid movement and collision between the substrate and enzyme.
pH
1.
2.
3.
Enzymes concentration The rate of reaction increase when the enzymes concentration is achieved. More enzymes are available when the concentration of the enzymes increase. Thus the rate of reaction increase if there are more substrate molecules available. After the maximum rate, the concentration of the substrate becomes the limiting factor.
Substrate concentration
1.
2.
3.
4.
An increase in substrate concentration will increase the rate of reaction until the reaction reaches a maximum rate. At low substrate concentrations, there are more enzymes molecules than substrate molecules. The rate of reaction increase because more active site are available. Therefore, an increase in substrate concentration will speed up the reaction if there are enough enzymes molecules to catalyst the substrate molecules.
5.
6.
7.
After the maximum rate , all the active sites of the enzymes molecules are occupied, so increasing the substrate concentration will not increase the rate of reaction. The rate of reaction becomes constant. Thus, the rate of reaction is directly proportional to the substrate concentration until the reaction reaches a maximum rate. The concentration of enzymes becomes a limiting factor.
1.
Enzymes are widely used in our homes and industries. Discuss how the enzymes are used in industries. (10 marks) Differentiate intracellular enzymes and extracellular enzymes. (2 marks) Explain how extracellular enzymes are produced. (8 marks)
2.
3.